CITE2_MOUSE
ID CITE2_MOUSE Reviewed; 269 AA.
AC O35740; O35741; O35742; O35743; O55198; Q6PGA9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cbp/p300-interacting transactivator 2;
DE AltName: Full=MSG-related protein 1;
DE Short=MRG-1;
DE AltName: Full=P35srj;
GN Name=Cited2; Synonyms=Mrg1, Msg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6 X DBA;
RX PubMed=9533950; DOI=10.1016/s0925-4773(98)00011-2;
RA Dunwoodie S.L., Rodriguez T.A., Beddington R.S.P.;
RT "Msg1 and Mrg1, founding members of a gene family, show distinct patterns
RT of gene expression during mouse embryogenesis.";
RL Mech. Dev. 72:27-40(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9434189; DOI=10.1016/s0378-1119(97)00551-9;
RA Shioda T., Fenner M.H., Isselbacher K.J.;
RT "MSG1 and its related protein MRG1 share a transcription activating
RT domain.";
RL Gene 204:235-241(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH LHX2.
RX PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
RA Glenn D.J., Maurer R.A.;
RT "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to
RT stimulate glycoprotein hormone alpha-subunit gene expression.";
RL J. Biol. Chem. 274:36159-36167(1999).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=11694877; DOI=10.1038/ng768;
RA Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
RA Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
RT "Cardiac malformations, adrenal agenesis, neural crest defects and
RT exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
RL Nat. Genet. 29:469-474(2001).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15051727; DOI=10.1074/jbc.m401489200;
RA Tien E.S., Davis J.W., Vanden Heuvel J.P.;
RT "Identification of the CREB-binding protein/p300-interacting protein CITED2
RT as a peroxisome proliferator-activated receptor alpha coregulator.";
RL J. Biol. Chem. 279:24053-24063(2004).
RN [10]
RP FUNCTION, ASSOCIATION WITH CHROMATIN, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15475956; DOI=10.1038/ng1446;
RA Bamforth S.D., Braganca J., Farthing C.R., Schneider J.E., Broadbent C.,
RA Michell A.C., Clarke K., Neubauer S., Norris D., Brown N.A., Anderson R.H.,
RA Bhattacharya S.;
RT "Cited2 controls left-right patterning and heart development through a
RT Nodal-Pitx2c pathway.";
RL Nat. Genet. 36:1189-1196(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
RX PubMed=16619037; DOI=10.1038/sj.onc.1209552;
RA Chou Y.T., Wang H., Chen Y., Danielpour D., Yang Y.C.;
RT "Cited2 modulates TGF-beta-mediated upregulation of MMP9.";
RL Oncogene 25:5547-5560(2006).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15750185; DOI=10.1242/dev.01696;
RA Weninger W.J., Lopes Floro K., Bennett M.B., Withington S.L., Preis J.I.,
RA Barbera J.P., Mohun T.J., Dunwoodie S.L.;
RT "Cited2 is required both for heart morphogenesis and establishment of the
RT left-right axis in mouse development.";
RL Development 132:1337-1348(2005).
RN [13]
RP FUNCTION, INTERACTION WITH WT1, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17537799; DOI=10.1242/dev.004390;
RA Val P., Martinez-Barbera J.P., Swain A.;
RT "Adrenal development is initiated by Cited2 and Wt1 through modulation of
RT Sf-1 dosage.";
RL Development 134:2349-2358(2007).
RN [14]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19457926; DOI=10.1093/hmg/ddp237;
RA Buaas F.W., Val P., Swain A.;
RT "The transcription co-factor CITED2 functions during sex determination and
RT early gonad development.";
RL Hum. Mol. Genet. 18:2989-3001(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21224256; DOI=10.1093/hmg/ddq554;
RA Lopes Floro K., Artap S.T., Preis J.I., Fatkin D., Chapman G.,
RA Furtado M.B., Harvey R.P., Hamada H., Sparrow D.B., Dunwoodie S.L.;
RT "Loss of Cited2 causes congenital heart disease by perturbing left-right
RT patterning of the body axis.";
RL Hum. Mol. Genet. 20:1097-1110(2011).
CC -!- FUNCTION: Transcriptional coactivator of the p300/CBP-mediated
CC transcription complex. Acts as a bridge, linking TFAP2 transcription
CC factors and the p300/CBP transcriptional coactivator complex in order
CC to stimulate TFAP2-mediated transcriptional activation. Positively
CC regulates TGF-beta signaling through its association with the
CC SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates
CC the peroxisome proliferator-activated receptors PPARA transcriptional
CC activity. Enhances estrogen-dependent transactivation mediated by
CC estrogen receptors. Acts also as a transcriptional corepressor;
CC interferes with the binding of the transcription factors HIF1A or STAT2
CC and the p300/CBP transcriptional coactivator complex. Participates in
CC sex determination and early gonad development by stimulating
CC transcription activation of SRY. Plays a role in controlling left-right
CC patterning during embryogenesis; potentiates transcriptional activation
CC of NODAL-mediated gene transcription in the left lateral plate mesoderm
CC (LPM). Plays an essential role in differentiation of the adrenal cortex
CC from the adrenogonadal primordium (AGP); stimulates WT1-mediated
CC transcription activation thereby up-regulating the nuclear hormone
CC receptor NR5A1 promoter activity. Associates with chromatin to the
CC PITX2 P1 promoter region. {ECO:0000269|PubMed:10593900,
CC ECO:0000269|PubMed:15475956, ECO:0000269|PubMed:15750185,
CC ECO:0000269|PubMed:16619037, ECO:0000269|PubMed:17537799,
CC ECO:0000269|PubMed:19457926, ECO:0000269|PubMed:21224256}.
CC -!- SUBUNIT: Interacts (via C-terminus) with EP300 (via CH1 domain); the
CC interaction is stimulated in response to hypoxia. Interacts with PPARA.
CC Interacts (via C-terminus) with TFAP2A, TFAP2B and TFAP2C (By
CC similarity). Interacts (via C-terminus) with SMAD2. Interacts (via C-
CC terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via LIM
CC domains). Interacts with WT1 isoform 1 and isoform 3. {ECO:0000250,
CC ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:16619037,
CC ECO:0000269|PubMed:17537799}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with EP300 in dot-like
CC structures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O35740-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35740-2; Sequence=VSP_001090;
CC Name=3;
CC IsoId=O35740-3; Sequence=VSP_001091;
CC Name=4;
CC IsoId=O35740-4; Sequence=VSP_001092;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15051727}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic heart. Expressed in the
CC ventral node, cardiac crescent and blood islands at 7.5 dpc. Expressed
CC in the cardiac crescent, anterior lateral mesoderm and in trunk
CC paraxial mesoderm at 8 dpc. Expressed in forebrain-midbrain boundary,
CC branchial arches 1 and 2, heart and somites at 9.5 dpc (at protein
CC level). Expressed in the coelomic epithelium and in cells in the
CC underlying nephrogenic mesenchyme of the genital ridge at 10 dpc.
CC Expressed in the genital ridge and the presumptive adrenal area at 10.5
CC dpc. Expressed in the gonad and in the adrenal anlagen at 12 dpc.
CC Expressed in the cells of the adrenal cortex at 14 dpc. Expressed
CC throughout the embryonic heart, as well as in the node and the lateral
CC plate mesoderm (LPM), that are responsible for initiating and
CC maintaining left-right patterning. Expressed in the crown cells of the
CC node. {ECO:0000269|PubMed:15475956, ECO:0000269|PubMed:15750185,
CC ECO:0000269|PubMed:17537799, ECO:0000269|PubMed:19457926}.
CC -!- DISRUPTION PHENOTYPE: Mice embryos die during gestation with left-right
CC patterning defects and severe developmental abnormalities, including
CC cardiac malformations, exencephaly and adrenal agenesis. Show also
CC impaired mesonephric tubules and adrenal cortex development in embryos.
CC {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:15475956,
CC ECO:0000269|PubMed:15750185, ECO:0000269|PubMed:17537799,
CC ECO:0000269|PubMed:21224256}.
CC -!- SIMILARITY: Belongs to the CITED family. {ECO:0000305}.
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DR EMBL; Y15163; CAA75432.1; -; mRNA.
DR EMBL; Y15163; CAA75433.1; -; mRNA.
DR EMBL; Y15163; CAA75434.1; -; mRNA.
DR EMBL; Y15163; CAA75435.1; -; mRNA.
DR EMBL; U86445; AAC39945.1; -; mRNA.
DR EMBL; AK131664; BAE20751.1; -; mRNA.
DR EMBL; AK133791; BAE21844.1; -; mRNA.
DR EMBL; AC105167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466562; EDL03481.1; -; Genomic_DNA.
DR EMBL; BC057126; AAH57126.1; -; mRNA.
DR CCDS; CCDS23708.1; -. [O35740-1]
DR RefSeq; NP_034958.2; NM_010828.3. [O35740-1]
DR AlphaFoldDB; O35740; -.
DR SMR; O35740; -.
DR BioGRID; 201524; 6.
DR MINT; O35740; -.
DR STRING; 10090.ENSMUSP00000038405; -.
DR iPTMnet; O35740; -.
DR PhosphoSitePlus; O35740; -.
DR EPD; O35740; -.
DR PaxDb; O35740; -.
DR PRIDE; O35740; -.
DR ProteomicsDB; 283845; -. [O35740-1]
DR ProteomicsDB; 283846; -. [O35740-2]
DR ProteomicsDB; 283847; -. [O35740-3]
DR ProteomicsDB; 283848; -. [O35740-4]
DR Antibodypedia; 4252; 272 antibodies from 34 providers.
DR DNASU; 17684; -.
DR Ensembl; ENSMUST00000038107; ENSMUSP00000038405; ENSMUSG00000039910. [O35740-1]
DR Ensembl; ENSMUST00000219558; ENSMUSP00000151452; ENSMUSG00000039910. [O35740-1]
DR GeneID; 17684; -.
DR KEGG; mmu:17684; -.
DR UCSC; uc007elt.2; mouse. [O35740-1]
DR CTD; 10370; -.
DR MGI; MGI:1306784; Cited2.
DR VEuPathDB; HostDB:ENSMUSG00000039910; -.
DR eggNOG; ENOG502QSRC; Eukaryota.
DR GeneTree; ENSGT00530000063624; -.
DR HOGENOM; CLU_090678_1_0_1; -.
DR InParanoid; O35740; -.
DR OMA; HAMGPGN; -.
DR OrthoDB; 1378769at2759; -.
DR TreeFam; TF331915; -.
DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 17684; 11 hits in 74 CRISPR screens.
DR ChiTaRS; Cited2; mouse.
DR PRO; PR:O35740; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O35740; protein.
DR Bgee; ENSMUSG00000039910; Expressed in metanephric cortical collecting duct and 292 other tissues.
DR ExpressionAtlas; O35740; baseline and differential.
DR Genevisible; O35740; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0050693; F:LBD domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0035802; P:adrenal cortex formation; IMP:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IMP:MGI.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0021602; P:cranial nerve morphogenesis; IMP:MGI.
DR GO; GO:0046697; P:decidualization; IMP:MGI.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IMP:BHF-UCL.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL.
DR GO; GO:0060972; P:left/right pattern formation; IBA:GO_Central.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0002521; P:leukocyte differentiation; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:BHF-UCL.
DR GO; GO:0008584; P:male gonad development; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:1900164; P:nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; IMP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:UniProtKB.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; IMP:MGI.
DR GO; GO:0003156; P:regulation of animal organ formation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
DR GO; GO:0034405; P:response to fluid shear stress; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007530; P:sex determination; IMP:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:BHF-UCL.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Differentiation;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..269
FT /note="Cbp/p300-interacting transactivator 2"
FT /id="PRO_0000144727"
FT REGION 142..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 138..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9533950"
FT /id="VSP_001090"
FT VAR_SEQ 159..213
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9434189,
FT ECO:0000303|PubMed:9533950"
FT /id="VSP_001091"
FT VAR_SEQ 203..213
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9533950"
FT /id="VSP_001092"
FT CONFLICT 194..195
FT /note="SG -> TC (in Ref. 1; CAA75432/CAA75435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28321 MW; 0FFCD8C21E4E3D81 CRC64;
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA
GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN
NQYFNHHPYP HNHYMPDLHP TAGHQMNGTN QHFRDCNPKH SGGSSTPGGA GGSGTPGGSG
GTSGGAGGSS AGGSGGGSTM PASVAHVPAA MLPPNVIDTD FIDEEVLMSL VIEMGLDRIK
ELPELWLGQN EFDFMTDFVC KQQPSRVSC
